KenHo said...
Close, but contains a few errors.
A protein depends on it's shape to be active. The shape is determined by the polypeptide sequence.
When a protein is denatured by heat or a few other things, it loses it's shape, and becomes inactive. If it returns to normal temperature, it regains it's shape, if the sequence is intact, which accounts for the return of pain.
Denaturing is not like scrambling an egg.
We could get into a very nerdy debate here.


As you are aware, the protein consists of a long polypeptide chain (or chains). This chain is then folded onto itself in a complex way to give the protein its "shape", referred to as secondary, tertiary, and quaternary structure. It is held in this shape by quite weak bonds (such as hydrogen bonds, salt bridges, non-polar hydrophobic interactions).
Heat and other insults (e.g. acids) breaks these weak bonds and allows the protein to unfold (i.e. change its shape). This occurs without breaking the polypeptide sequence or chain (which is held together by stronger covalent bonds). New bonds then form which hold it in this new shape even when the temperature returns back to normal. The shape of the protein molecule has changed but its polypeptide sequence has not. This process is called denaturation.
To reverse this denaturation requires energy to break these weak bonds again and also a replication of the conditions under which the protein was first formed inside the fish cell (e.g. temperature, pH, concentrations of various electrolytes, other solutes, plus/minus enzymes). Without these specific conditions, even with the application of energy to get over the unfavorable kinetics, the protein will not return to its original shape.
Hence denaturation (=change in shape) by heat is usually irreversible. The egg being an obvious example.
However, might it be conceivable that with very low heat only a couple of the weakest bonds break, leaving almost all of the "shape" intact so that it could possibly return back to its original "shape" spontaneously? Such a minor loss in shape might be just enough if it were to occur at the right place for it not to be able to interact with whatever it needs to in the foot (such as bind to pain receptors, or act as an enzyme to catalyze a specific reaction).
There would be a whole heap of other plausible sounding explanations of how heat changes the multiple biological processes that occur in the foot that finally result in the activation of pain nerve fibres.
I think we simply don't know for sure.